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HEADER HYDROLASE/HYDROLASE INHIBITOR 05-AUG-14 4R1D
TITLE THE CRYSTAL STRUCTURE OF TLE4-TLI4 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: UNP RESIDUES 33-380;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: PA1510;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 10 ORGANISM_TAXID: 208964;
SOURCE 11 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 12 GENE: PA1509;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LU
REVDAT 1 17-DEC-14 4R1D 0
JRNL AUTH D.LU,Y.ZHENG,N.LIAO,L.WEI,B.XU,X.LIU,J.LIU
JRNL TITL THE STRUCTURAL BASIS OF THE TLE4-TLI4 COMPLEX REVEALS THE
JRNL TITL 2 SELF-PROTECTION MECHANISM OF H2-T6SS IN PSEUDOMONAS
JRNL TITL 3 AERUGINOSA.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 3233 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 25478841
JRNL DOI 10.1107/S1399004714023967
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 86321
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 4331
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 20.0043 - 5.4003 0.99 2899 161 0.1726 0.2001
REMARK 3 2 5.4003 - 4.3004 0.99 2884 159 0.1438 0.1677
REMARK 3 3 4.3004 - 3.7609 0.96 2766 147 0.1511 0.1790
REMARK 3 4 3.7609 - 3.4189 0.96 2778 158 0.1686 0.2107
REMARK 3 5 3.4189 - 3.1749 0.98 2836 131 0.1790 0.2130
REMARK 3 6 3.1749 - 2.9883 0.98 2854 136 0.1906 0.2206
REMARK 3 7 2.9883 - 2.8391 0.97 2793 156 0.1798 0.2307
REMARK 3 8 2.8391 - 2.7158 0.97 2839 155 0.1755 0.1959
REMARK 3 9 2.7158 - 2.6115 0.97 2774 153 0.1803 0.2184
REMARK 3 10 2.6115 - 2.5216 0.97 2816 181 0.1809 0.2399
REMARK 3 11 2.5216 - 2.4429 0.97 2828 134 0.1787 0.1909
REMARK 3 12 2.4429 - 2.3732 0.97 2803 135 0.1701 0.2236
REMARK 3 13 2.3732 - 2.3108 0.97 2779 119 0.1649 0.2002
REMARK 3 14 2.3108 - 2.2545 0.95 2789 153 0.1680 0.2128
REMARK 3 15 2.2545 - 2.2033 0.95 2760 144 0.1691 0.2153
REMARK 3 16 2.2033 - 2.1565 0.96 2752 146 0.1758 0.2372
REMARK 3 17 2.1565 - 2.1134 0.94 2750 135 0.1838 0.2455
REMARK 3 18 2.1134 - 2.0735 0.95 2754 130 0.1842 0.2659
REMARK 3 19 2.0735 - 2.0365 0.93 2698 162 0.1859 0.2441
REMARK 3 20 2.0365 - 2.0020 0.93 2654 149 0.1928 0.2435
REMARK 3 21 2.0020 - 1.9698 0.93 2661 154 0.1925 0.2456
REMARK 3 22 1.9698 - 1.9395 0.92 2664 145 0.1868 0.2565
REMARK 3 23 1.9395 - 1.9110 0.92 2651 123 0.1963 0.2517
REMARK 3 24 1.9110 - 1.8841 0.91 2633 148 0.1964 0.2244
REMARK 3 25 1.8841 - 1.8587 0.91 2620 134 0.1996 0.2355
REMARK 3 26 1.8587 - 1.8345 0.92 2691 136 0.2112 0.2803
REMARK 3 27 1.8345 - 1.8116 0.90 2550 153 0.2091 0.2457
REMARK 3 28 1.8116 - 1.7898 0.90 2634 131 0.2156 0.2377
REMARK 3 29 1.7898 - 1.7690 0.88 2544 127 0.2171 0.2644
REMARK 3 30 1.7690 - 1.7491 0.88 2536 136 0.2385 0.2994
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 37.93
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43250
REMARK 3 B22 (A**2) : -0.19640
REMARK 3 B33 (A**2) : 0.62890
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.21010
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 6707
REMARK 3 ANGLE : 1.065 9120
REMARK 3 CHIRALITY : 0.076 947
REMARK 3 PLANARITY : 0.005 1209
REMARK 3 DIHEDRAL : 14.103 2505
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4R1D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-14.
REMARK 100 THE RCSB ID CODE IS RCSB086776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86321
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.749
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M BIS-TRIS PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 67.58950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 5
REMARK 465 LEU A 6
REMARK 465 GLU A 7
REMARK 465 PRO A 8
REMARK 465 ASN A 9
REMARK 465 GLN A 10
REMARK 465 ASP A 11
REMARK 465 VAL A 12
REMARK 465 ILE A 13
REMARK 465 ILE A 14
REMARK 465 PRO A 15
REMARK 465 ARG A 16
REMARK 465 SER A 17
REMARK 465 ARG A 18
REMARK 465 ASP A 19
REMARK 465 SER A 20
REMARK 465 LEU A 21
REMARK 465 GLY A 22
REMARK 465 ARG A 23
REMARK 465 PRO A 24
REMARK 465 VAL A 25
REMARK 465 TYR A 26
REMARK 465 LYS A 27
REMARK 465 ALA A 28
REMARK 465 GLN A 29
REMARK 465 LEU A 30
REMARK 465 THR A 31
REMARK 465 ARG A 32
REMARK 465 THR A 33
REMARK 465 ASP A 34
REMARK 465 ASN A 35
REMARK 465 GLN A 36
REMARK 465 SER A 37
REMARK 465 GLU A 38
REMARK 465 LYS A 39
REMARK 465 VAL A 40
REMARK 465 ALA A 41
REMARK 465 LEU A 42
REMARK 465 ILE A 43
REMARK 465 ARG A 44
REMARK 465 HIS A 562
REMARK 465 PRO A 563
REMARK 465 ASN A 564
REMARK 465 ASP A 565
REMARK 465 LYS A 566
REMARK 465 GLY A 567
REMARK 465 GLY A 568
REMARK 465 THR A 569
REMARK 465 SER B 334
REMARK 465 SER B 335
REMARK 465 PRO B 336
REMARK 465 ARG B 337
REMARK 465 GLY B 338
REMARK 465 GLY B 339
REMARK 465 ASN B 340
REMARK 465 ALA B 341
REMARK 465 GLY B 342
REMARK 465 PRO B 343
REMARK 465 SER B 344
REMARK 465 PRO B 345
REMARK 465 ALA B 346
REMARK 465 PRO B 347
REMARK 465 LYS B 348
REMARK 465 PRO B 349
REMARK 465 ALA B 350
REMARK 465 THR B 351
REMARK 465 PRO B 352
REMARK 465 GLY B 353
REMARK 465 GLY B 354
REMARK 465 GLN B 355
REMARK 465 THR B 356
REMARK 465 LEU B 357
REMARK 465 GLY B 358
REMARK 465 ASP B 359
REMARK 465 HIS B 360
REMARK 465 TYR B 361
REMARK 465 VAL B 362
REMARK 465 TYR B 363
REMARK 465 GLU B 364
REMARK 465 GLU B 365
REMARK 465 PHE B 366
REMARK 465 LEU B 367
REMARK 465 SER B 368
REMARK 465 SER B 369
REMARK 465 LEU B 370
REMARK 465 LYS B 371
REMARK 465 PRO B 372
REMARK 465 LYS B 373
REMARK 465 ASP B 374
REMARK 465 SER B 375
REMARK 465 TRP B 376
REMARK 465 LEU B 377
REMARK 465 ASP B 378
REMARK 465 ASP B 379
REMARK 465 LEU B 380
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 73 80.65 -154.06
REMARK 500 MET A 81 71.31 -67.12
REMARK 500 TRP A 94 -58.55 -136.79
REMARK 500 LEU A 106 60.55 -100.46
REMARK 500 TRP A 167 -53.21 77.57
REMARK 500 ASP A 170 -75.45 -150.35
REMARK 500 SER A 256 -133.54 57.77
REMARK 500 ILE A 369 -56.38 -125.26
REMARK 500 LYS A 393 -34.26 -38.23
REMARK 500 GLU A 426 67.35 -117.64
REMARK 500 GLU A 498 -36.89 97.43
REMARK 500 LYS B 35 30.16 -95.94
REMARK 500 GLU B 109 9.47 57.64
REMARK 500 ASP B 189 23.82 -140.32
REMARK 500 ASN B 302 65.59 38.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1120 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A1275 DISTANCE = 6.77 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 202 O
REMARK 620 2 GLU A 152 OE2 104.2
REMARK 620 3 ASP A 203 OD1 74.0 84.1
REMARK 620 4 ASP A 156 OD1 78.0 125.9 143.5
REMARK 620 5 ASP A 156 OD2 124.9 91.6 161.1 51.3
REMARK 620 6 HOH A 796 O 153.8 74.0 79.8 124.8 81.2
REMARK 620 7 HOH A 811 O 93.6 151.6 79.7 79.1 96.2 80.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601
DBREF 4R1D A 1 569 UNP Q9I3K2 Q9I3K2_PSEAE 1 569
DBREF 4R1D B 33 380 UNP Q9I3K3 Q9I3K3_PSEAE 33 380
SEQRES 1 A 569 MET SER SER GLU PRO LEU GLU PRO ASN GLN ASP VAL ILE
SEQRES 2 A 569 ILE PRO ARG SER ARG ASP SER LEU GLY ARG PRO VAL TYR
SEQRES 3 A 569 LYS ALA GLN LEU THR ARG THR ASP ASN GLN SER GLU LYS
SEQRES 4 A 569 VAL ALA LEU ILE ARG GLN THR ALA PRO LEU PRO VAL ILE
SEQRES 5 A 569 PHE ILE PRO GLY ILE MET GLY THR ASN LEU ARG ASN LYS
SEQRES 6 A 569 ALA ASP LYS SER GLU VAL TRP ARG PRO PRO ASN GLY LEU
SEQRES 7 A 569 TRP PRO MET ASP ASP LEU PHE ALA SER ILE GLY ALA LEU
SEQRES 8 A 569 TRP THR TRP ALA TRP ARG GLY PRO LYS ALA ARG GLN GLU
SEQRES 9 A 569 LEU LEU LYS ALA GLU GLN VAL GLU VAL ASP ASP GLN GLY
SEQRES 10 A 569 THR ILE ASP VAL GLY GLN SER GLY LEU SER GLU GLU ALA
SEQRES 11 A 569 ALA ARG LEU ARG GLY TRP GLY LYS VAL MET ARG SER ALA
SEQRES 12 A 569 TYR ASN PRO VAL MET GLY LEU MET GLU ARG ARG LEU ASP
SEQRES 13 A 569 ASN ILE VAL SER ARG ARG GLU LEU GLN ALA TRP TRP ASN
SEQRES 14 A 569 ASP GLU ALA LEU SER PRO PRO GLY ASP GLN GLY GLU GLU
SEQRES 15 A 569 GLN GLY LYS VAL GLY PRO ILE ASP GLU GLU GLU LEU LEU
SEQRES 16 A 569 ARG ALA SER ARG TYR GLN PHE ASP VAL TRP CYS ALA GLY
SEQRES 17 A 569 TYR ASN TRP LEU GLN SER ASN ARG GLN SER ALA LEU ASP
SEQRES 18 A 569 VAL ARG ASP TYR ILE GLU ASN THR VAL LEU PRO PHE TYR
SEQRES 19 A 569 GLN LYS GLU CYS GLY LEU ASP PRO GLU GLN MET ARG ARG
SEQRES 20 A 569 MET LYS VAL ILE LEU VAL THR HIS SER MET GLY GLY LEU
SEQRES 21 A 569 VAL ALA ARG ALA LEU THR GLN LEU HIS GLY TYR GLU ARG
SEQRES 22 A 569 VAL LEU GLY VAL VAL HIS GLY VAL GLN PRO ALA THR GLY
SEQRES 23 A 569 SER SER THR ILE TYR HIS HIS MET ARG CYS GLY TYR GLU
SEQRES 24 A 569 GLY ILE ALA GLN VAL VAL LEU GLY ARG ASN ALA GLY GLU
SEQRES 25 A 569 VAL THR ALA ILE VAL ALA ASN SER ALA GLY ALA LEU GLU
SEQRES 26 A 569 LEU ALA PRO SER ALA GLU TYR ARG GLU GLY ARG PRO TRP
SEQRES 27 A 569 LEU PHE LEU CYS ASP ALA GLN GLY GLN VAL LEU LYS ASP
SEQRES 28 A 569 ILE ASP GLY LYS PRO ARG ALA TYR PRO GLN ASN GLN ASP
SEQRES 29 A 569 PRO TYR GLU GLU ILE TYR LYS ASN THR THR TRP TYR GLY
SEQRES 30 A 569 LEU VAL PRO GLU GLN ASN SER GLN TYR LEU ASP MET SER
SEQRES 31 A 569 ASP LYS LYS GLU GLY LEU ARG VAL GLY PRO ARG ASP ASN
SEQRES 32 A 569 PHE GLU ASP LEU ILE ASP SER ILE ALA ASN PHE HIS GLY
SEQRES 33 A 569 GLU LEU SER ALA ALA GLY TYR HIS SER GLU THR TYR ALA
SEQRES 34 A 569 HIS TYR GLY ALA ASP ASP SER ARG HIS SER TRP ARG ASP
SEQRES 35 A 569 LEU ILE TRP LYS GLY ASP PRO THR PRO LEU GLU THR PRO
SEQRES 36 A 569 GLY ALA THR LEU ASN ASP ASP GLU ASN GLY THR TYR ASN
SEQRES 37 A 569 SER TRP PHE ARG ARG GLY LEU PRO THR ILE VAL GLN GLY
SEQRES 38 A 569 PRO LEU GLU THR GLY ASN PRO LEU ASP ALA SER GLY SER
SEQRES 39 A 569 GLY GLY ASP GLU THR VAL PRO THR ASP SER GLY GLN ALA
SEQRES 40 A 569 PRO ALA LEU ALA GLY VAL LYS ALA SER PHE ARG HIS GLY
SEQRES 41 A 569 SER LYS GLY LYS GLY GLN ALA ASN THR LYS ARG GLY TYR
SEQRES 42 A 569 GLU HIS GLN GLU SER TYR ASN ASP ALA ARG ALA GLN TRP
SEQRES 43 A 569 ALA ALA LEU TYR GLY VAL ILE LYS ILE THR GLN LEU ALA
SEQRES 44 A 569 ASP TRP HIS PRO ASN ASP LYS GLY GLY THR
SEQRES 1 B 348 MET ASP LYS THR GLY TRP ILE THR HIS CYS PHE GLY ARG
SEQRES 2 B 348 PHE LEU ILE ASP LEU PRO PRO ASP ALA VAL ILE ASN ALA
SEQRES 3 B 348 GLY TYR TYR LEU TRP GLY ASP ARG ILE GLU TYR LEU ASP
SEQRES 4 B 348 ASP LYS PRO THR GLU LEU ALA ALA ARG VAL ASP ARG LEU
SEQRES 5 B 348 GLU GLN GLU TRP ARG THR GLN ARG HIS LYS SER LYS GLY
SEQRES 6 B 348 ASN MET PHE LEU ARG LYS ILE ASP PHE GLY ASN GLU SER
SEQRES 7 B 348 VAL GLY LEU LEU SER TRP SER SER GLU VAL ALA SER LYS
SEQRES 8 B 348 THR TYR LEU LEU ASP THR TYR VAL THR SER LYS PRO THR
SEQRES 9 B 348 TRP HIS VAL TYR ARG TRP LYS GLY LYS VAL SER VAL ASP
SEQRES 10 B 348 ARG GLU GLN HIS ALA VAL GLU ILE SER ARG ALA LEU ALA
SEQRES 11 B 348 ARG ASN LEU ARG SER ARG ALA PRO LYS GLU ILE PRO SER
SEQRES 12 B 348 GLU PRO GLY PHE CYS ILE ASP HIS ALA TYR ILE ALA GLY
SEQRES 13 B 348 ASP SER PHE GLN VAL GLU ARG PHE GLY VAL GLY VAL THR
SEQRES 14 B 348 PHE PRO GLU HIS PRO GLY ALA ARG PHE GLU PHE ARG SER
SEQRES 15 B 348 SER THR GLY ALA GLU LEU ASN SER LEU LEU GLU ARG VAL
SEQRES 16 B 348 ASP GLY PHE VAL GLN ASN MET LEU SER THR PHE ALA GLY
SEQRES 17 B 348 MET GLU THR LEU ARG LYS GLY LYS HIS PRO VAL GLY SER
SEQRES 18 B 348 LEU PRO GLY GLU GLU TYR LEU VAL ALA GLY SER ASP LYS
SEQRES 19 B 348 GLY GLN ARG GLY TYR THR PHE MET TRP GLU VAL GLN GLY
SEQRES 20 B 348 LYS GLU GLU SER LEU THR GLU PRO ASN LEU THR ALA GLY
SEQRES 21 B 348 LEU ALA VAL LEU GLU ARG SER ASN GLU ASN GLY LYS PRO
SEQRES 22 B 348 PRO PRO PRO ALA PHE LYS SER ASP LYS GLU ALA LEU GLU
SEQRES 23 B 348 LEU TRP ASP THR ILE VAL ASP SER ILE ARG VAL ARG PRO
SEQRES 24 B 348 THR SER SER SER PRO ARG GLY GLY ASN ALA GLY PRO SER
SEQRES 25 B 348 PRO ALA PRO LYS PRO ALA THR PRO GLY GLY GLN THR LEU
SEQRES 26 B 348 GLY ASP HIS TYR VAL TYR GLU GLU PHE LEU SER SER LEU
SEQRES 27 B 348 LYS PRO LYS ASP SER TRP LEU ASP ASP LEU
HET CA A 601 1
HETNAM CA CALCIUM ION
FORMUL 3 CA CA 2+
FORMUL 4 HOH *960(H2 O)
HELIX 1 1 ASP A 83 TRP A 94 1 12
HELIX 2 2 GLY A 98 LEU A 106 1 9
HELIX 3 3 LYS A 107 GLU A 109 5 3
HELIX 4 4 SER A 127 ARG A 134 1 8
HELIX 5 5 GLY A 135 VAL A 139 5 5
HELIX 6 6 MET A 140 ASP A 156 1 17
HELIX 7 7 ASP A 170 SER A 174 5 5
HELIX 8 8 PRO A 175 GLY A 180 5 6
HELIX 9 9 ASP A 190 SER A 198 1 9
HELIX 10 10 SER A 214 THR A 229 1 16
HELIX 11 11 THR A 229 GLY A 239 1 11
HELIX 12 12 ASP A 241 MET A 248 1 8
HELIX 13 13 MET A 257 LEU A 268 1 12
HELIX 14 14 SER A 288 GLY A 297 1 10
HELIX 15 15 ASN A 309 ALA A 318 1 10
HELIX 16 16 SER A 320 GLU A 325 1 6
HELIX 17 17 GLU A 331 ARG A 336 5 6
HELIX 18 18 ASP A 364 ILE A 369 1 6
HELIX 19 19 PRO A 380 LEU A 387 5 8
HELIX 20 20 LYS A 392 LEU A 396 5 5
HELIX 21 21 GLY A 399 GLY A 422 1 24
HELIX 22 22 PRO A 449 THR A 454 1 6
HELIX 23 23 ASN A 487 SER A 494 5 8
HELIX 24 24 PRO A 501 GLN A 506 1 6
HELIX 25 25 GLN A 506 ALA A 511 1 6
HELIX 26 26 GLU A 537 ASN A 540 5 4
HELIX 27 27 ASP A 541 GLN A 557 1 17
HELIX 28 28 LYS B 73 GLN B 91 1 19
HELIX 29 29 ARG B 150 ASN B 164 1 15
HELIX 30 30 SER B 222 PHE B 238 1 17
HELIX 31 31 SER B 312 ASP B 325 1 14
SHEET 1 A 6 GLN A 201 CYS A 206 0
SHEET 2 A 6 PRO A 48 ILE A 54 1 N PHE A 53 O TRP A 205
SHEET 3 A 6 VAL A 250 HIS A 255 1 O VAL A 253 N ILE A 54
SHEET 4 A 6 VAL A 274 GLY A 280 1 O LEU A 275 N VAL A 250
SHEET 5 A 6 THR A 427 GLY A 432 1 O TYR A 428 N VAL A 277
SHEET 6 A 6 ALA A 515 HIS A 519 1 O ALA A 515 N ALA A 429
SHEET 1 B 3 GLU A 70 TRP A 72 0
SHEET 2 B 3 LEU A 62 ASN A 64 -1 N LEU A 62 O VAL A 71
SHEET 3 B 3 VAL A 111 VAL A 113 -1 O GLU A 112 N ARG A 63
SHEET 1 C 2 VAL A 159 SER A 160 0
SHEET 2 C 2 GLU A 163 LEU A 164 -1 O GLU A 163 N SER A 160
SHEET 1 D 4 ALA A 358 TYR A 359 0
SHEET 2 D 4 LEU A 339 CYS A 342 -1 N LEU A 339 O TYR A 359
SHEET 3 D 4 LEU A 443 LYS A 446 1 O LEU A 443 N PHE A 340
SHEET 4 D 4 THR A 477 VAL A 479 -1 O THR A 477 N LYS A 446
SHEET 1 E 3 ILE B 39 PHE B 43 0
SHEET 2 E 3 PHE B 46 LEU B 50 -1 O LEU B 50 N ILE B 39
SHEET 3 E 3 ARG B 328 VAL B 329 -1 O ARG B 328 N LEU B 47
SHEET 1 F12 PHE B 100 ASP B 105 0
SHEET 2 F12 VAL B 111 TRP B 116 -1 O LEU B 114 N ARG B 102
SHEET 3 F12 THR B 124 THR B 132 -1 O TYR B 130 N VAL B 111
SHEET 4 F12 VAL B 139 SER B 147 -1 O VAL B 146 N TYR B 125
SHEET 5 F12 ASP B 65 LEU B 70 -1 N GLU B 68 O ARG B 141
SHEET 6 F12 VAL B 55 LEU B 62 -1 N LEU B 62 O ASP B 65
SHEET 7 F12 GLU B 194 THR B 201 -1 O ARG B 195 N TYR B 61
SHEET 8 F12 ALA B 208 SER B 215 -1 O PHE B 210 N VAL B 200
SHEET 9 F12 ASN B 288 VAL B 295 -1 O GLY B 292 N GLU B 211
SHEET 10 F12 GLN B 268 VAL B 277 -1 N PHE B 273 O LEU B 293
SHEET 11 F12 GLU B 257 ASP B 265 -1 N GLY B 263 O GLY B 270
SHEET 12 F12 MET B 241 LYS B 248 -1 N ARG B 245 O LEU B 260
SHEET 1 G 3 LEU B 165 SER B 167 0
SHEET 2 G 3 ALA B 184 ALA B 187 -1 O TYR B 185 N ARG B 166
SHEET 3 G 3 GLY B 178 ILE B 181 -1 N PHE B 179 O ILE B 186
LINK O PHE A 202 CA CA A 601 1555 1555 2.39
LINK OE2 GLU A 152 CA CA A 601 1555 1555 2.42
LINK OD1 ASP A 203 CA CA A 601 1555 1555 2.47
LINK OD1 ASP A 156 CA CA A 601 1555 1555 2.52
LINK OD2 ASP A 156 CA CA A 601 1555 1555 2.59
LINK CA CA A 601 O HOH A 796 1555 1555 2.57
LINK CA CA A 601 O HOH A 811 1555 1555 2.64
CISPEP 1 GLN A 45 THR A 46 0 4.49
CISPEP 2 PRO A 74 PRO A 75 0 2.89
CISPEP 3 TRP A 79 PRO A 80 0 -8.82
CISPEP 4 TYR A 359 PRO A 360 0 -3.58
CISPEP 5 GLY A 481 PRO A 482 0 4.26
CISPEP 6 LYS B 134 PRO B 135 0 -0.41
SITE 1 AC1 6 GLU A 152 ASP A 156 PHE A 202 ASP A 203
SITE 2 AC1 6 HOH A 796 HOH A 811
CRYST1 59.681 135.179 62.606 90.00 113.49 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016756 0.000000 0.007283 0.00000
SCALE2 0.000000 0.007398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017416 0.00000
TER 4112 TRP A 561
TER 6532 SER B 333
MASTER 387 0 1 31 33 0 2 6 7422 2 9 71
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